Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases

ABSTRACT: Background: RNA post-transcriptional modification is an exciting field of research that has evidenced this editing process as a sophisticated epigenetic mechanism to fine tune the ribosome function and to control gene expression. Although tRNA modifications seem to be more relevant for the...

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Autores:
Mosquera Rendón, Jeanneth
Cárdenas Brito, Sonia
Pineda Cárdenas, Juan David
Corredor Rodríguez, Mauricio
Benítez Páez, Alfonso
Tipo de recurso:
Article of investigation
Fecha de publicación:
2014
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/22179
Acceso en línea:
http://hdl.handle.net/10495/22179
Palabra clave:
Evolución Molecular
Evolution, Molecular
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Bacteria
Bacterias
RNA methyltransferases
Conserved sequence motifs
Rights
openAccess
License
http://creativecommons.org/licenses/by/2.5/co/
id UDEA2_7de8abab3d11cf0cb462394f8effa07f
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/22179
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
title Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
spellingShingle Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
Evolución Molecular
Evolution, Molecular
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Bacteria
Bacterias
RNA methyltransferases
Conserved sequence motifs
title_short Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
title_full Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
title_fullStr Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
title_full_unstemmed Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
title_sort Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases
dc.creator.fl_str_mv Mosquera Rendón, Jeanneth
Cárdenas Brito, Sonia
Pineda Cárdenas, Juan David
Corredor Rodríguez, Mauricio
Benítez Páez, Alfonso
dc.contributor.author.none.fl_str_mv Mosquera Rendón, Jeanneth
Cárdenas Brito, Sonia
Pineda Cárdenas, Juan David
Corredor Rodríguez, Mauricio
Benítez Páez, Alfonso
dc.subject.decs.none.fl_str_mv Evolución Molecular
Evolution, Molecular
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Bacteria
Bacterias
topic Evolución Molecular
Evolution, Molecular
Farmacorresistencia Microbiana
Drug Resistance, Microbial
Bacteria
Bacterias
RNA methyltransferases
Conserved sequence motifs
dc.subject.proposal.spa.fl_str_mv RNA methyltransferases
Conserved sequence motifs
description ABSTRACT: Background: RNA post-transcriptional modification is an exciting field of research that has evidenced this editing process as a sophisticated epigenetic mechanism to fine tune the ribosome function and to control gene expression. Although tRNA modifications seem to be more relevant for the ribosome function and cell physiology as a whole, some rRNA modifications have also been seen to play pivotal roles, essentially those located in central ribosome regions. RNA methylation at nucleobases and ribose moieties of nucleotides appear to frequently modulate its chemistry and structure. RNA methyltransferases comprise a superfamily of highly specialized enzymes that accomplish a wide variety of modifications. These enzymes exhibit a poor degree of sequence similarity in spite of using a common reaction cofactor and modifying the same substrate type. Results: Relationships and lineages of RNA methyltransferases have been extensively discussed, but no consensus has been reached. To shed light on this topic, we performed amino acid and codon-based sequence analyses to determine phylogenetic relationships and molecular evolution. We found that most Class I RNA MTases are evolutionarily related to protein and cofactor/vitamin biosynthesis methyltransferases. Additionally, we found that at least nine lineages explain the diversity of RNA MTases. We evidenced that RNA methyltransferases have high content of polar and positively charged amino acid, which coincides with the electrochemistry of their substrates. Conclusions: After studying almost 12,000 bacterial genomes and 2,000 patho-pangenomes, we revealed that molecular evolution of Class I methyltransferases matches the different rates of synonymous and non-synonymous substitutions along the coding region. Consequently, evolution on Class I methyltransferases selects against amino acid changes affecting the structure conformation
publishDate 2014
dc.date.issued.none.fl_str_mv 2014
dc.date.accessioned.none.fl_str_mv 2021-09-04T01:54:35Z
dc.date.available.none.fl_str_mv 2021-09-04T01:54:35Z
dc.type.spa.fl_str_mv info:eu-repo/semantics/article
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dc.type.local.spa.fl_str_mv Artículo de investigación
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dc.identifier.citation.spa.fl_str_mv Mosquera, J., Cárdenas, S., Pineda, J., Corredor, M., & Benítez, A. (2014) Relaciones evolutivas y basadas en secuencias en metiltransferasas de ARN no codificantes dependientes de AdoMet bacterianas. BMC Res Notes 7, 440. https://doi.org/10.1186/1756-0500-7-440
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/10495/22179
dc.identifier.doi.none.fl_str_mv 10.1186/1756-0500-7-440
dc.identifier.eissn.none.fl_str_mv 1756-0500
identifier_str_mv Mosquera, J., Cárdenas, S., Pineda, J., Corredor, M., & Benítez, A. (2014) Relaciones evolutivas y basadas en secuencias en metiltransferasas de ARN no codificantes dependientes de AdoMet bacterianas. BMC Res Notes 7, 440. https://doi.org/10.1186/1756-0500-7-440
10.1186/1756-0500-7-440
1756-0500
url http://hdl.handle.net/10495/22179
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.ispartofjournalabbrev.spa.fl_str_mv BMC Res. Notes.
dc.rights.spa.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/co/
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https://creativecommons.org/licenses/by-nc-nd/4.0/
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dc.publisher.spa.fl_str_mv BMC
dc.publisher.group.spa.fl_str_mv GEBIOMIC (Genética y Bioquímica de Microorganismos)
dc.publisher.place.spa.fl_str_mv Londres, Inglaterra
institution Universidad de Antioquia
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spelling Mosquera Rendón, JeannethCárdenas Brito, SoniaPineda Cárdenas, Juan DavidCorredor Rodríguez, MauricioBenítez Páez, Alfonso2021-09-04T01:54:35Z2021-09-04T01:54:35Z2014Mosquera, J., Cárdenas, S., Pineda, J., Corredor, M., & Benítez, A. (2014) Relaciones evolutivas y basadas en secuencias en metiltransferasas de ARN no codificantes dependientes de AdoMet bacterianas. BMC Res Notes 7, 440. https://doi.org/10.1186/1756-0500-7-440http://hdl.handle.net/10495/2217910.1186/1756-0500-7-4401756-0500ABSTRACT: Background: RNA post-transcriptional modification is an exciting field of research that has evidenced this editing process as a sophisticated epigenetic mechanism to fine tune the ribosome function and to control gene expression. Although tRNA modifications seem to be more relevant for the ribosome function and cell physiology as a whole, some rRNA modifications have also been seen to play pivotal roles, essentially those located in central ribosome regions. RNA methylation at nucleobases and ribose moieties of nucleotides appear to frequently modulate its chemistry and structure. RNA methyltransferases comprise a superfamily of highly specialized enzymes that accomplish a wide variety of modifications. These enzymes exhibit a poor degree of sequence similarity in spite of using a common reaction cofactor and modifying the same substrate type. Results: Relationships and lineages of RNA methyltransferases have been extensively discussed, but no consensus has been reached. To shed light on this topic, we performed amino acid and codon-based sequence analyses to determine phylogenetic relationships and molecular evolution. We found that most Class I RNA MTases are evolutionarily related to protein and cofactor/vitamin biosynthesis methyltransferases. Additionally, we found that at least nine lineages explain the diversity of RNA MTases. We evidenced that RNA methyltransferases have high content of polar and positively charged amino acid, which coincides with the electrochemistry of their substrates. Conclusions: After studying almost 12,000 bacterial genomes and 2,000 patho-pangenomes, we revealed that molecular evolution of Class I methyltransferases matches the different rates of synonymous and non-synonymous substitutions along the coding region. Consequently, evolution on Class I methyltransferases selects against amino acid changes affecting the structure conformationCOL001406415application/pdfengBMCGEBIOMIC (Genética y Bioquímica de Microorganismos)Londres, Inglaterrainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARTArtículo de investigaciónhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/co/http://purl.org/coar/access_right/c_abf2https://creativecommons.org/licenses/by-nc-nd/4.0/Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferasesEvolución MolecularEvolution, MolecularFarmacorresistencia MicrobianaDrug Resistance, MicrobialBacteriaBacteriasRNA methyltransferasesConserved sequence motifsBMC Res. Notes.BMC Research Notes1157440CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8927http://bibliotecadigital.udea.edu.co/bitstream/10495/22179/2/license_rdf1646d1f6b96dbbbc38035efc9239ac9cMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/22179/3/license.txt8a4605be74aa9ea9d79846c1fba20a33MD53ORIGINALMosqueraJeanneth_EvolutionalBacterialAdoMet.pdfMosqueraJeanneth_EvolutionalBacterialAdoMet.pdfArtículo de investigaciónapplication/pdf2089635http://bibliotecadigital.udea.edu.co/bitstream/10495/22179/1/MosqueraJeanneth_EvolutionalBacterialAdoMet.pdf8448927ab06dc6a7d6c588174884557cMD5110495/22179oai:bibliotecadigital.udea.edu.co:10495/221792021-09-03 20:54:36.195Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.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